作者: Ivan Duran , Jorge H Martin , Mary Ann Weis , Pavel Krejci , Peter Konik
DOI: 10.1002/JBMR.3095
关键词:
摘要: Lysine hydroxylation of type I collagen telopeptides varies from tissue to tissue, and these distinct patterns modulate cross-linking generate a unique extracellular matrix. Abnormalities in contribute pathologies that include osteogenesis imperfecta (OI), fibrosis, cancer. Telopeptide procollagen modifications are carried out by lysyl hydroxylase 2 (LH2); however, little is known regarding how this enzyme regulates patterns. We identified an ER complex resident chaperones includes HSP47, FKBP65, BiP regulating the activity LH2. Our findings show FKBP65 HSP47 LH2 either favor or repress its activity. was also as member complex, playing role enhancing formation complex. This newly chaperone contributes our understanding C-telopeptides affect quality connective tissues. © 2017 American Society for Bone Mineral Research.